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Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis.
Strunk, Robert J; Piemonte, Katrina M; Petersen, Natasha M; Koutsioulis, Dimitris; Bouriotis, Vassilis; Perry, Kay; Cole, Kathryn E.
Afiliação
  • Strunk RJ; Department of Chemistry, Ithaca College, 953 Danby Road, Ithaca, NY 14850, USA.
  • Piemonte KM; Department of Chemistry, Ithaca College, 953 Danby Road, Ithaca, NY 14850, USA.
  • Petersen NM; Department of Chemistry, Ithaca College, 953 Danby Road, Ithaca, NY 14850, USA.
  • Koutsioulis D; Department of Biology, Enzyme Biotechnology Group, University of Crete, PO Box 2209, Vassilika Vouton, 71409 Heraklion, Crete, Greece.
  • Bouriotis V; Department of Biology, Enzyme Biotechnology Group, University of Crete, PO Box 2209, Vassilika Vouton, 71409 Heraklion, Crete, Greece.
  • Perry K; Northeastern Collaborative Access Team (NE-CAT) and Department of Chemistry and Chemical Biology, Cornell University, Building 436E, Argonne National Laboratory, 9700 South Cass Avenue, Argonne, IL 60439, USA.
  • Cole KE; Department of Chemistry, Ithaca College, 953 Danby Road, Ithaca, NY 14850, USA.
Acta Crystallogr F Struct Biol Commun ; 70(Pt 2): 156-9, 2014 Feb.
Article em En | MEDLINE | ID: mdl-24637747
ABSTRACT
Polysaccharide deacetylases are bacterial enzymes that catalyze the deacetylation of acetylated sugars on the membranes of Gram-positive bacteria, allowing them to be unrecognized by host immune systems. Inhibition of these enzymes would disrupt such pathogenic defensive mechanisms and therefore offers a promising route for the development of novel antibiotic therapeutics. Here, the first X-ray crystal structure of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis, is reported to 2.0 Å resolution. The overall structure maintains the conserved (α/ß)8 fold that is characteristic of this family of enzymes. The lack of a catalytic metal ion and a distinctive metal-binding site, however, suggest that this enzyme is not a functional polysaccharide deacetylase.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bacillus anthracis / Amidoidrolases Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Ano de publicação: 2014 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bacillus anthracis / Amidoidrolases Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Ano de publicação: 2014 Tipo de documento: Article